Steroidogenic activity of a peptide specified by the reversed sequence of corticotropin mRNA

Benjamin L. Clarke, J. Edwin Blalock

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The molecular recognition theory predicts that a reversed (3'→5') reading of an mRNA should yield a peptide that is structurally and functionally similar to that specified in the 5'→3' direction. We tested this idea by synthesizing a corticotropin (ACTH) analogue using a reverse reading of bovine mRNA for ACTH-(1-24). This peptide, designated ACTH-3'→5', had a similar hydropathic profile to native ACTH-5'→3' but had only 30% sequence homology and eight different charge substitutions. ACTH-3'→5' specifically bound to the surface of mouse Y-1 adrenal cells and to polyclonal anti-ACTH antibody. Additionally, ACTH-3'→5' stimulated cAMP synthesis and steroidogenesis in adrenal cells. These findings show that ACTH-3'→5' mimics the corticotropic properties of native ACTH, thereby further validating the molecular recognition theory.

Original languageEnglish (US)
Pages (from-to)9708-9711
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number24
DOIs
StatePublished - 1990

Keywords

  • antisense peptide
  • complementary peptide
  • molecular code
  • molecular recognition theory
  • peptide mimetic

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